Clinical Significance Of MUC1

Clinical Significance Of MUC1

The extracellular domain of MUC1 (MUC1 antibody) is heavily glycosylated, which prevents chemotherapy medicines from reaching cancer cells. The glycosylation creates a highly hydrophilic area that hinders the passage of hydrophobic chemotherapy medicines. This keeps the medications from reaching their intended targets, which are normally found inside the cell. Glycosylation has also been found to bind to growth factors. This enables cancer cells that make a lot of MUC1 to concentrate growth factors near their receptors, resulting in increased receptor activity and cancer cell proliferation. Through steric hindrance, MUC1 also hinders immune cells from interacting with receptors on the cancer cell surface. This suppresses the immune system's anti-tumor response.

The cytoplasmic tail of MUC1 has been discovered to interact to p53. Genotoxic stress amplifies this connection. The p53 response region of the p21 gene promoter was discovered to be related to MUC1 and p53. This causes p21 to become activated, which causes cell cycle arrest. In cancer, MUC1 interacts with p53, inhibiting p53-mediated apoptosis and promoting p53-mediated cell cycle arrest. Hence by so doing it prevents cell death.

Beta-catenin interacts with the cytoplasmic tail of MUC1. MUC1 contains an SXXXXXSSL motif that is shared by various beta-catenin binding partners. Cell adhesion was found to be necessary for this interaction. MUC1 is phosphorylated on a YEKV motif, according to research. LYN, through the mediation of interleukin 7, Src, through the mediation of EGFR, and PRKCD, have all shown phosphorylation of this location.